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Literature summary extracted from

  • Sinhababu, A.K.; Bartel, R.L.; Pochopin, N.; Borchardt, R.T.
    Mechanism of action of S-adenosyl-L-homocysteine hydrolase. Measurement of kinetic isotope effects using adenosine-3'-d and S-adenosyl-L-homocysteine-3'-d as substrates (1985), J. Am. Chem. Soc., 107, 7628-7632.
No PubMed abstract available

Application

EC Number Application Comment Organism
3.13.2.1 medicine chemotherapeutic drug design Bos taurus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.13.2.1 S-adenosyl-L-homocysteine + H2O Bos taurus
-
 adenosine + L-homocysteine
-
 r

Organism

EC Number Organism UniProt Comment Textmining
3.13.2.1 Bos taurus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.13.2.1 partial Bos taurus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.13.2.1 liver
-
 Bos taurus
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.13.2.1 12
-
-
 Bos taurus

Storage Stability

EC Number Storage Stability Organism
3.13.2.1 -20°C Bos taurus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.13.2.1 DL-homocysteine + adenosine
-
 Bos taurus S-adenosyl-DL-homocysteine
-
 r
3.13.2.1 S-adenosyl-L-homocysteine + H2O
-
 Bos taurus adenosine + L-homocysteine
-
 r

Cofactor

EC Number Cofactor Comment Organism Structure
3.13.2.1 NAD+
-
 Bos taurus